BCH 361

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Anonymous
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264778
Filename:
BCH 361
Updated:
2014-03-02 21:19:14
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bch361
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science
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  1. What did the fox say?
    Ding ding ding
  2. Which force are involved in maintaining the primary structure of a
    protein?
    Covalent Bonds
  3. 1)      Which
    one is NOT an example of supersecondary structure?

    A)    The
    pyrrole ring

    B)    The
    greek key

    C)    The
    beta meander

    D)    The
    beta barrel
    A. The pyrolle key
  4. 1)      The
    amount of energy released during a reaction tells nothing about the rate at
    which that reaction will occur.

    A)    True

    B)    False
    A. True
  5. 1)      The
    following methods are useful for cell homogenization:

    A)    Sonication

    B)    Freezing
    and Thawing

    C)    Detergents

    D)    Enzymes

    E)     All
    of the above
    E. All of the above
  6. 1)      Which
    separates based on molecular weight?

    A)    Gel
    filtration

    B)    Affinity
    chromatography

    C)    Cation
    exchange

    D)    Anion
    exchange

    E)     Cation
    or anion exchange
    A. Gel Filtration
  7.  

    1)      A
    separation of a mixture of cations requires:

    A)    Another
    cationic substance

    B)    An
    anionic substance

    C)    An
    electrically neutral, but slightly polar substance

    D)    An
    electrically neutral, nonpolar substance
    B. An anionic substance
  8. 1)      The
    following are all principles of electrophoresis, except:

    A)    Molecular
    size

    B)    pI

    C)    Net
    charge

    D)    Binding
    to substrate
    D. Binding to substrate
  9. 1)      All
    catalysts work by lowering the activation energy of the reaction.

    A)    True

    B)    False
    A. True
  10. 1)      When
    the substrate concentration is low, the an enzyme reaction

    A)    Will
    display zero order kinetics

    B)    Will
    display first order kinetics

    C)    Will
    display second order kinetics

    D)    Will
    denature and cease to function
    Will Display first order kinetics
  11. 1)      A
    lineweaver-burk plot is useful in the analysis of enzymatic reactions because

    A)    It
    is easier to see if points deviate from a straight line, instead of a curve

    B)    It
    allows you to calculate the exact values from a straight line

    C)    It
    is an easy way to manipulate the data into a useful form

    D)    All
    of the above
    D. All of the above
  12.  

    1)       The value of Vmax change in

    A)    Competitive
    inhibition

    B)    Noncompetitive
    inhibition

    C)    Both
    forms

    D)    None
    of the above
    B. Non-competitive Inhibition
  13.  

    1)       Generally speaking, a competitive inhibitor
    and the substrate cannot both bind to the enzyme at the same time.

    A)    True

    B)    False
    TRUE
  14. 1)       The Michaelis-menton constant determines the
    Vmax of an enzymatic reaction.

    A)    True

    B)    False
    FALSE
  15.  

    1)       What types of macromolecules are usually
    separated on agarose gel electrophoresis gels?
    Nucleic Acids (DNA)
  16. Are
    all enzymes proteins?
    No but most are. There are some catalytic RNA's known.
  17. 1)      What
    are the elements of secondary structure in proteins?  Pick one of these elements and outline in
    detail the main characteristics of this form of secondary structure.  Pay special attention to the forces involved,
    and the arrangement of the structure.
    • Alpha Helix:
    • Stabilized by hydrogen bonds parallel to helix axis within backbone.
    • R Groups point out from Helix

    • B Sheet:
    • Hydrogen Bonds are perpendicular to axis of sheet
    • R Groups alternate above and below plane of sheet.
  18.  

    1)       Explain in detail the significance of Km.
    • Km is a measure of affinity for substrate and enzyme.
    • Increase of Km = more dissociation and less affinity
    • Decrease of Km = less dissociation and more affinity
  19. Using
    a diagram of a basic tertiary structure, show three of the five forces that
    stabilize this level of protein structure. 
    You MUST be specific, showing interacting atoms.
    Look it up
  20. Detail
    the structural features of Secondary Structure in Proteins.
    double
  21. How
    does the lock and key model of enzyme-substrate binding differ from the induced
    fit model?
    • Lock and key model: substrate binds to
    • that portion of the enzyme with a complementary shape.

    • Induce fit model: Binding of the
    • substrate induces a change in the conformation of the enzyme that results in a
    • complementary fit.
  22. Describe
    in detail, how column chromatography work. 
    What components need to be present to run this sort of a
    separation?  Define all terms.
    • Column chromatography works to separate out
    • components of a mixture, through different interactions with a stationary
    • phase. The stationary phase is typically a polymer with linkers attached to it.
    • The stationary phase interacts with the components of the sampe and leads to separation.
    • The mobile phase contains the mixture, usually Ph a buffer and passes over the
    • stationary phase.

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